ID K9SM42_9CYAN Unreviewed; 637 AA.
AC K9SM42;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AFY71046.1};
GN ORFNames=Pse7367_2793 {ECO:0000313|EMBL:AFY71046.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY71046.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY71046.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY71046.1,
RC ECO:0000313|Proteomes:UP000010386};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR EMBL; CP003592; AFY71046.1; -; Genomic_DNA.
DR RefSeq; WP_015166002.1; NC_019701.1.
DR AlphaFoldDB; K9SM42; -.
DR STRING; 82654.Pse7367_2793; -.
DR KEGG; pseu:Pse7367_2793; -.
DR PATRIC; fig|82654.3.peg.3271; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_000288_135_5_3; -.
DR OrthoDB; 9788659at2; -.
DR Proteomes; UP000010386; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AFY71046.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000010386};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:AFY71046.1};
KW Transferase {ECO:0000313|EMBL:AFY71046.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 384..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 278..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 637 AA; 69068 MW; 45A610808EE32D2C CRC64;
MSGNLLNNRY RIIEVLGSGG FGETFLAEDT QMPSLRRCVI KQLKPIANNP LVYHLVKERF
QREAAVLEKL GDEHRQIPRL YAKFNENGLF YLVQEWIDGQ TLAAKVYEEG LFDEAIARQV
LVEVLLVLDF VHGQGMIHRD IKPDNIIMRQ GDRLPVLIDF GSVKETLGTV VNVPNAQGQT
TTSIVIGTPG FMPTEQAAGR PVFASDIYSL GMTIIYAITG KIPRELPIDL ETGRVRWQEY
ASHLSTELIA ILDRATQVYS RDRYANAREM LNDLQPRWQT GLQGSGNSQA STGQGNIGSG
QNIQSHSGAA ANQASGVNSG QNNLSNTGQS SSTTTPAHPT QTNQPIATRL QQTQQPQSSQ
RSQRSGNSPA RSSAQGNEPA DRQITLLTAI VASGIASLLV VLGVLALNSR LTARKPVPAI
NNPAPTAPGQ NPNQPTTVPT VEQPNAPNQP IDRELAAELE KRSQIDQSCQ DDTSREVKII
APQSPLDVHM RPSIDAQVTA SLPNGSTAGV VSSQGDWLEI NSPVNGWIDR SATTSNCDRQ
VEAISFAPNQ SSTTISSSFE VPGSHAYIVR ANAGQVLVLQ QLQGSLPILK DPNGQLVASA
NRNGDRAAFR LSASGIYTLE FSSVEPDYIY EFSLQLE
//
